L-ARABINOFURANOSYLATED PROBES FOR THE ANALYSIS OF NOVEL L-ARABINOFURANOSIDASES FROM BIFIDOBACTERIUM LONGUM

摘要

The L-arabinofuranosylated oligosaccharide has been found in the indigestible dietary fibers such as plant cell wall glycoconjugates. In the non-reducing terminal end of glycan in the glycoconjugates such as hydroxyproline-rich glycoproteins (HRGPs), ss-L-arabinofuranoside (ss-L-Araf) is existed. The O-glycan linked to Hyp in HRGP is oligo-Larabinofuranoside (L-Araf_(1-4)) including ss-L-Araf which is hydrolyzed by L-arabinofuranosidases (L-Arafases) [1] isolated from the human gastrointestinal bacterium, Bifidobacterim longum, including a novel ss-L-Arafase, HypBA1 (GH127). The other ss-L-arabinofuranosylated motifs have been also found in plant arabinan whose structures might be also cleaved by other unknown ss-L-Arafases [2]. To analyze the catalytic mechanism of the GH127 ss-L-Arafase, we would like to present our synthetic study of various L-arabinofuranosylated probes.